DAHP synthase

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase (EC 2.5.1.54) is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan.

A series of catalytic mechanisms result in the production of aromatic amino acids required for metabolism.

[3] In Escherichia coli, a species of bacteria, DAHP synthase is found as three isoenzymes, each of which sensitive to one of the amino acids produced in the shikimate pathway.

[3] Since DAHP synthase is required for the production of essential aromatic amino acids such as tyrosine, phenylalanine, and tryptophan.

Inhibition could potentially act as an antimicrobial for specific parasites such as Toxoplasma gondii, Plasmodium falciparum, and Cryptosporidium parvum.

Stabilization of the transition state increases the affinity for the inhibitor, effectively inhibiting DAHP synthase from functioning.

Researchers continue to study methods of inhibition of the shikimate pathway to prevent the growth of parasitic microbes.

Inhibiting the first enzyme of this pathway would prevent vital amino acids from being synthesized, halting the production of proteins and slowing growth.

[2] In DAHP synthase, it has been shown that binding site contains patterns of cysteine and histidine residues bound to metal ions in a Cys-X-X-His fashion.

[2] It has been shown that, in general, DAHP synthases require a bivalent metal ion cofactor in order for the enzyme to function properly.